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From Proteopedia
Contents |
genetics is ok
'Molecules it Interacts With and where '
The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
PHENYLALANINE
MAGNESIUM ION
'Origin'
It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.
'Structure'
It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.
Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.
'Molecules it Interacts With and where '
The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
PHENYLALANINE
MAGNESIUM ION
'Origin'
It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.
'Structure'
It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.
Specific are highlighted here.
which play a crucial role in binding to the ribosome during translation.
'Function"
The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.
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Introduction
The catabolite activator protein (CAP) is a transcription activator in both eukaryotes and prokaryotes. CAP activates transcription by engaging in interactions with the α-subunit of RNA polymerase. CAP's name comes from its ability to affect the transcription of genes involved in several catabolic pathways.
Structure
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Function
CAPs interact with RNA Polymerase, which causes DNA to bend near the transcription start site. This interaction then catalyzes the initiation process of transcription.
Disease
Relevance
Structural Highlights
Each CAP subunit is made of a cAMP-binding domain at the N-terminus and a DNA-binding domain at the C-terminus. The allows the CAP to form a complex with cAMP (cyclic adenosine monophosphate) which leads to the activation of transcription at many different promoters. The includes a helix-turn-helix motif structure, which allows CAP to bind to successive major grooves of DNA, effectively opening up the DNA molecule and allowing room for RNA polymerase to bind. These two domains are connected by a , which is a long alpha helix that is involved in the conformational change induced by cAMP.
